A diiron protein autogenerates a valine-phenylalanine cross-link.
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ABSTRACT:
SUBMITTER: Cooley RB
PROVIDER: S-EPMC3736988 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Publications
A diiron protein autogenerates a valine-phenylalanine cross-link.
Cooley Richard B RB Rhoads Timothy W TW Arp Daniel J DJ Karplus P Andrew PA
Science (New York, N.Y.) 20110501 6032
All known internal covalent cross-links in proteins involve functionalized groups having oxygen, nitrogen, or sulfur atoms present to facilitate their formation. Here, we report a carbon-carbon cross-link between two unfunctionalized side chains. This valine-phenyalanine cross-link, produced in an oxygen-dependent reaction, is generated by its own carboxylate-bridged diiron center and serves to stabilize the metallocenter. This finding opens the door to new types of posttranslational modificatio ...[more]
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